BMRB Entry 18445
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18445
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Title: NMR high resolution structures of free Tah1 and Tah1 bound to the Hsp90 C-terminal tail explain how Hsp90 recognizes the R2TP complex PubMed: 24012479
Deposition date: 2012-05-07 Original release date: 2013-05-20
Authors: BACK, Regis; DOMINGUEZ, Cyril; ROTHE, Benjamin; BOBO, Claude; BEAUFILS, Chrystel; MORERA, Solange; MEYER, Philippe; CHARPENTIER, Bruno; BRANLANT, Christiane; ALLAIN, Frederic H.-T.; MANIVAL, Xavier
Citation: Back, Regis; Dominguez, Cyril; Rothe, Benjamin; Bobo, Claude; Beaufils, Chrystel; Morera, Solange; Meyer, Philippe; Charpentier, Bruno; Branlant, Christiane; Allain, Frederic H-T; Manival, Xavier. "High-resolution structural analysis shows how Tah1 tethers Hsp90 to the R2TP complex." Structure 21, 1834-1847 (2013).
Assembly members:
entity, polymer, 110 residues, 12393.052 Da.
Natural source: Common Name: bakers yeast Taxonomy ID: 4932 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Saccharomyces cerevisiae
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: SQFEKQKEQGNSLFKQGLYR
EAVHCYDQLITAQPQNPVGY
SNKAMALIKLGEYTQAIQMC
QQGLRYTSTAEHVAIRSKLQ
YRLELAQGAVGSVQIPVVEV
DELPEGYDRS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 327 |
| 1H chemical shifts | 760 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | yeast Tah1 | 1 |
Entities:
Entity 1, yeast Tah1 110 residues - 12393.052 Da.
| 1 | SER | GLN | PHE | GLU | LYS | GLN | LYS | GLU | GLN | GLY | |
| 2 | ASN | SER | LEU | PHE | LYS | GLN | GLY | LEU | TYR | ARG | |
| 3 | GLU | ALA | VAL | HIS | CYS | TYR | ASP | GLN | LEU | ILE | |
| 4 | THR | ALA | GLN | PRO | GLN | ASN | PRO | VAL | GLY | TYR | |
| 5 | SER | ASN | LYS | ALA | MET | ALA | LEU | ILE | LYS | LEU | |
| 6 | GLY | GLU | TYR | THR | GLN | ALA | ILE | GLN | MET | CYS | |
| 7 | GLN | GLN | GLY | LEU | ARG | TYR | THR | SER | THR | ALA | |
| 8 | GLU | HIS | VAL | ALA | ILE | ARG | SER | LYS | LEU | GLN | |
| 9 | TYR | ARG | LEU | GLU | LEU | ALA | GLN | GLY | ALA | VAL | |
| 10 | GLY | SER | VAL | GLN | ILE | PRO | VAL | VAL | GLU | VAL | |
| 11 | ASP | GLU | LEU | PRO | GLU | GLY | TYR | ASP | ARG | SER |
Samples:
sample_1: Tah1, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 10 mM; sodium chloride 150 mM; H2O 90%; D2O 10%
sample_2: Tah1, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 10 mM; sodium chloride 150 mM; D2O 150 mM
sample_conditions_1: ionic strength: 160 mM; pH: 7.2; pressure: 1 atm; temperature: 288 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection
SPARKY, Goddard - chemical shift assignment
AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 750 MHz